Recombinant Human Dedicator of cytokinesis protein 8 (DOCK8) is produced using a yeast expression system and covers amino acids 560 to 729. This partial protein carries an N-terminal 10xHis tag that helps with purification and detection. The product shows purity levels above 85%, confirmed through SDS-PAGE analysis. This protein is meant for research use only and should not be used for diagnostic or therapeutic purposes.
The Dedicator of cytokinesis protein 8 (DOCK8) appears to be involved in cellular processes that reorganize the cytoskeleton. It likely plays a critical role in immune system function, particularly within signaling pathways that control cell migration and survival. Given its apparent importance in immune cell dynamics, DOCK8 has become a significant focus for studies examining immunodeficiencies and related immune conditions.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Protein-Protein Interaction Studies
This recombinant DOCK8 fragment (560-729aa) works well in pull-down assays for identifying and characterizing binding partners within this specific domain region. The N-terminal 10xHis tag allows immobilization on nickel-affinity resins, which can then capture interacting proteins from cell lysates or purified protein libraries. These studies might help map the interaction network of this DOCK8 domain and may reveal binding specificities. While the yeast expression system provides proper eukaryotic folding, it also maintains cost-effectiveness for interaction screening experiments.
2. Antibody Development and Validation
The purified DOCK8 fragment can work as an immunogen or screening antigen when developing domain-specific antibodies against the 560-729aa region. High purity (>85%) and the His-tag help with both immunization protocols and later antibody validation through ELISA or Western blot analyses. Researchers might use this fragment to generate antibodies that specifically recognize this DOCK8 domain without cross-reacting to other regions of the full-length protein. The defined amino acid boundaries should allow for precise epitope mapping studies.
3. Structural and Biophysical Characterization
This DOCK8 domain fragment offers suitable material for structural biology approaches, including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy studies. The purified protein works in biophysical analyses such as dynamic light scattering, circular dichroism spectroscopy, or thermal stability assays to characterize folding properties and stability of this specific domain. The His-tag helps with purification optimization for structural studies. Meanwhile, the yeast expression system may provide appropriate post-translational modifications for native-like folding.
4. Biochemical Assay Development
The recombinant DOCK8 fragment can serve as a reference standard or positive control in biochemical assays designed to study DOCK8 function or regulation. Researchers can develop binding assays, enzymatic activity measurements, or inhibitor screening platforms using this purified domain as a substrate or target protein. The consistent quality and purity should enable reproducible assay conditions across different experimental batches. The His-tag allows for straightforward immobilization in plate-based assay formats or biosensor applications.
